| Title : Protein Crystallography and Site-Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis - Liu_2018_Chembiochem_19_1471 |
| Author(s) : Liu B , He L , Wang L , Li T , Li C , Liu H , Luo Y , Bao R |
| Ref : Chembiochem , 19 :1471 , 2018 |
|
Abstract :
Unlike traditional recycling strategies, biodegradation is a sustainable solution for disposing of poly(ethylene terephthalate) (PET) waste. PETase, a newly identified enzyme from Ideonella sakaiensis, has high efficiency and specificity towards PET and is, thus, a prominent candidate for PET degradation. On the basis of biochemical analysis, we propose that a wide substrate-binding pocket is critical for its excellent ability to hydrolyze crystallized PET. Structure-guided site-directed mutagenesis revealed an improvement in PETase catalytic efficiency, providing valuable insight into how the molecular engineering of PETase can optimize its application in biocatalysis. |
| PubMedSearch : Liu_2018_Chembiochem_19_1471 |
| PubMedID: 29603535 |
| Gene_locus related to this paper: idesa-peth |
| Gene_locus | idesa-peth |
| Structure | 5YFE |
Liu B, He L, Wang L, Li T, Li C, Liu H, Luo Y, Bao R (2018)
Protein Crystallography and Site-Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis
Chembiochem
19 :1471
Liu B, He L, Wang L, Li T, Li C, Liu H, Luo Y, Bao R (2018)
Chembiochem
19 :1471